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Crystal structure of the complex between S-adenosyl homocysteine and methanocaldococcus jannaschi DIM1.

Analyse Crystal structure of the complex between S-adenosyl homocysteine and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GRR
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dimethyladenosine transferase
EC: 2.1.1.-
UniProt: Q58435
Ligands: SAH
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dimethyladenosine transferase (EC 2.1.1.-)	protein	263	49% helix, 19% strand	Q58435

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	222	0.68	0.85	38	SAH
2	66	0.31	0.74	12	empty

Compared structures

3GRR · Crystal Structure of the complex between S-Adenosyl Homocysteine and Methanocaldococcus… · the same entry in another collection · chain A against A, TM-score 1.00
Q58435 · AlphaFold monomer V2.0 prediction for probable ribosomal RNA small subunit… · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q58435
Elsewhere: RCSB PDB 3GRR · PDBe 3GRR · UniProt Q58435

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